JPH03294298A - Acylated substance of vegetable protein polypeptide or salt thereof - Google Patents

Abstract

NEW MATERIAL:A compound expressed by the formula (R1 is 7-21C alkyl, 7-21C alkenyl or hydrocarbon of an alicyclic structure; R2 is side chain of constituent amino acid in plant protein peptides; n is 2-30; M is H, alkali metal such as Li, Na or K or onium such as ammonium or organic amine such as monoethanolamine, diethanolamine or 2-amino-2-methylpropane). USE:A base for cosmetics such as shampoo or lotion. PREPARATION:A plant protein polypeptide is acylated with a higher fatty acid (e.g. caprylic acid) having a 7-21C alkyl group or 7-21C alkenyl group or resin acid, etc., at pH8-10 and 20-50 deg.C for 1-6hr.

Description

DETAILED DESCRIPTION OF THE INVENTION [Field of Industrial Application] The present invention relates to an acylated product of a plant protein polypeptide or a salt thereof.

[Conventional technology]

Animal proteins such as collagen and keratin
The fact that the hydrolyzate (polypeptide) of
It has also been reported in Publication No. 8358. This is because the hydrolysates of these animal proteins have chemical structures similar to those of hair and skin, and they attach to the hair through their amino and carboxyl groups, or through the action of the side chains of the constituent amino acids, causing the hair to become damaged. This is thought to be due to its protective and regenerating effects.

[The problem that the invention attempts to solve]

However, since animal proteins such as collagen and keratin are used as starting materials from living animals, their supply is limited. There is a problem that we need to find out.

In addition, although these animal protein hydrolysates are useful for hair protection and regeneration as mentioned above, protein derivatives other than animal proteins also have the same effect on hair as such animal protein hydrolysates. It is necessary to develop new compounds that have properties that are not available in animal protein hydrolysates.

[Means for solving problems]

The present invention acylates a plant protein polypeptide obtained by hydrolyzing a plant protein with an acid having an alicyclic structure such as a higher fatty acid or a resin acid, thereby making use of the characteristics of the plant protein polypeptide. The present invention provides a novel compound that has surfactant properties not found in peptides and is useful as a compounding agent for hair cosmetics and skin cosmetics.

That is, the present invention provides - formula (■): 0 R2 R+ CnNHCHCOhnOeMΦ (in the formula, R,
is an alkyl group having 7 to 21 carbon atoms, an alkenyl group having 7 to 21 carbon atoms, or a hydrocarbon group having an alicyclic structure, and R is a side chain of a constituent amino acid of the plant protein polypeptide.

n is 2 to 30, M is hydrogen, an alkali metal such as lithium, sodium, potassium, ammonium or monoethanolamine, jetanolamine, triethanolamine, 2-amino-2-methylpropane, 2-amino-2 The present invention relates to an acylated product of a plant protein polypeptide or a salt thereof.

Examples of the vegetable protein that is the raw material for obtaining the acylated product of the plant protein polypeptide represented by formula (r) or its salt include, for example, cereals, beans, seeds,
Proteins such as buckwheat (buckwheat noodles) and seaweed, please be specific.
For example, wheat, pigeon wheat, rye, barley, oats (unrivaled), corn, soybeans, almonds, cashews, sesame seeds, peanuts, buckwheat, wakame (young cloth).
Examples include proteins obtained from plants or their processed products, such as Amanori (seed seaweed), Iwanori (rock seaweed), Kawanori (dried seaweed), and Matsumo (pine algae).

In addition, in formula (I) above, amino acids whose side chains are represented by R include alanine, glycine, valine, leucine, isoleucine, proline, phenylalanine, tyrosine, serine, threonine, methionine, arginine, histidine, and lysine. , aspartic acid, asparagine, glutamic acid, glutamine, cystine, tryptophan, etc. Table 1 shows an analysis example of the composition ratio of these amino acids.

In Table 1, asparagine and glutamine are included in aspartic acid and glutamic acid, respectively. Since cystine has two amino groups and two carboxyl groups, the composition ratio is expressed as half cystine in Table 1.

Such an acylated product of a plant protein polypeptide represented by formula (I) or a salt thereof has excellent surfactant ability based on the acylation of the carboxyl group at the terminal end of the peptide, and can be used with general surfactants. However, unlike ordinary synthetic surfactants, they are derived from natural plant proteins, so they are extremely irritating to the skin and mucous membranes, and have no effect. Very calm. In addition, it contains the same peptide components as skin and hair, so it has a gentle effect on skin and hair.
It does not damage the skin or hair (exhibits an excellent cleaning effect).Furthermore, the acylated product of the plant protein polypeptide or its salt represented by the above-mentioned formula (I) is composed of a plant protein component and an oil and fat component. It is adsorbed to the hair by the action of the amino groups and carboxyl groups in the plant protein components, as well as the chains of various amino acids.
Peptide components and oils and fats necessary for hair can be supplied at the same time. The acylated product of the plant protein polypeptide or its salt represented by formula (I) is
It has the effect of protecting the skin and hair and regenerating damaged hair derived from the peptide component, and has excellent effects such as adding luster and luster and improving hair combability derived from the oil component. Therefore, for example, it is included in various hair cosmetics such as shampoo, hair conditioner, styling foam, hair conditioner, hair back, hair liquid, hair back, and permanent wave agent for the purpose of hair protection, conditioning, and nutritional supplementation. , can exhibit its excellent effects. In addition, it is less irritating to the skin and mucous membranes, and since plant proteins have a good affinity for the skin, oils and fats have a good affinity for the skin, and strong surfactants can remove oils and fats from the skin. It prevents excess skin from coming off, moisturizes the skin, protects the skin, and prevents dryness, so it can be effectively used as a base ingredient in cosmetics such as Low Silan, Cleansing Low Citan, Naging Low Ci5, and various creams. It has a high night-time effect as a drug.

In addition, as shown in Table 1, the plant protein that is the raw material for the acylated product of the plant protein polypeptide represented by the above general formula (1) or its salt has a large amount of glutamic acid and aspartic acid in its constituent amino acids. Therefore, the acylated product of the plant protein polypeptide represented by the above general formula (I) or its salt exhibits stronger detergency and trapping power than the acylated product of animal protein polypeptide such as collagen or its salt. do. In addition, the moisturizing power, etc.
It is superior to acylated animal protein polypeptides or salts thereof, and has an excellent effect on improving skin feel.

The acylated product of the plant protein polypeptide represented by the above general formula (r) or its salt is obtained by acylating the plant protein polypeptide with higher fatty acids, resin acids, etc. Peptides can be obtained by hydrolyzing plant proteins using acids, alkalis, or proteolytic enzymes. During hydrolysis, by appropriately selecting the amount of acid, alkali, or enzyme to be added, reaction temperature, and reaction time, the value of n of the obtained plant protein polypeptide can be adjusted to 2 to 30, that is, the molecular weight can be adjusted to approximately 300 to approximately 300. 4,50
The preferred value can be 0.

Acid hydrolysis, alkaline hydrolysis, and enzymatic hydrolysis of plant proteins are carried out as follows.

(1) Hydrolysis with acids Examples of acids include inorganic acids such as hydrochloric acid, sulfuric acid, phosphoric acid, nitric acid, and hydrobromic acid, and organic acids such as acetic acid and formic acid.
IF can be given. Hydrochloric acid and acetic acid may also be used as a mixture, and these are generally used at a concentration of 5 to 85% (hereinafter, the concentration is %, unless a standard is indicated, it is a weighted %). However, the hydrolysis reaction always occurs at pH 4.
It is desirable that the reaction temperature is as follows. If more acid is used than necessary, the hue of the hydrolyzate solution becomes brown, which is undesirable. The reaction temperature is preferably 40 to 100"C, but 160"C under pressure. The reaction time is preferably 2 to 24 hours.The reactant can be neutralized with an alkali such as sodium hydroxide, potassium hydroxide, or sodium carbonate and used as is, but the reactant or neutralized product can be used as is. It can also be used after being purified by gel filtration, ion exchange resin, ultrafiltration, dialysis, electrodialysis, etc.

(2) Hydrolysis with alkali As the alkali, for example, inorganic alkalis such as sodium hydroxide, potassium hydroxide, lithium hydroxide, barium hydroxide, sodium carbonate, potassium carbonate, and lithium carbonate are used. These are generally suitable at concentrations of 1 to 20%. If more alkali is used than necessary, the hue of the hydrolyzate solution will turn brown to black, so it is preferable to carry out the undesirable 0 reaction at a temperature of room temperature to 100°C for 30 minutes to 24 hours. Care must be taken not to raise the level too high or make the reaction time too long. Hydrolysis with an alkali has the advantage that the hydrolyzate of the plant protein is eluted as the reaction progresses, making the progress of the reaction visible.The reaction can be terminated when the reaction mixture becomes a homogeneous solution. After the reaction, neutralize with the acid mentioned above, or
Or gel filtration, ion exchange FI! Preferably, purification is carried out using resins, ultrafiltration, dialysis, electrodialysis, and the like.

(3) Examples of enzymatic hydrolases include acidic proteolytic enzymes such as pepsin, protase A, and protase B, papain,
Neutral or alkaline proteolytic enzymes such as bromelain, thermolysin, trypsin, pronase, and chymotrypsin are used. Further, neutral or alkaline proteolytic enzymes such as subtilisin and staphylococcal protease can also be used. p during hydrolysis
H is p in the case of acidic proteolytic enzymes such as pepsin.
In the case of papain and other neutral to alkaline proteolytic enzymes, it is preferable to adjust the pH to a range of 4 to 10.The pH is generally adjusted using a buffer such as an acetic acid/sodium acetate buffer or a phosphate buffer. or acid,
The reaction temperature, which is preferably adjusted appropriately by addition of an alkali or the like, is preferably 30 to 45°C, and the reaction time is generally 3 to 24 hours.

In a hydrolysis reaction using an enzyme, the molecular weight of the hydrolyzate is greatly influenced by the amount of enzyme used, reaction temperature, and reaction time. Therefore, in order to obtain a plant protein polypeptide with the desired molecular weight, the molecular weight distribution of the obtained hydrolyzate should be investigated using the gel filtration method under each condition of the amount of enzyme used, reaction temperature, and reaction time, and the optimal conditions should be determined. It is preferable to decide.

Polypeptides obtained by enzymatic hydrolysis are
Compared to polypeptides obtained by hydrolysis with acids or alkalis, it has a narrower molecular weight distribution and produces fewer free amino acids, so it is suitable for use in cosmetics.

The average molecular weight of the polypeptide obtained by these hydrolysis is preferably 300 to 4.500. The adsorption ability of the plant protein polypeptide to hair is determined by its molecular weight, and the average molecular weight is 300 to 1,000.
This is because those with an average molecular weight of more than 4,500 are most easily adsorbed and easily soluble in water, and are easy to handle. This molecular weight range of 300 to 4,500 corresponds to n of 2 to 30 in the general formula (1).

Note that since the plant protein polypeptides obtained by hydrolyzing plant proteins are obtained in the form of a mixture of molecules having different molecular weights, the above n is expressed as an average value.

On the other hand, as a component for acylating a plant protein polypeptide, an alkyl group having 7 to 21 carbon atoms or an alkenyl group having 7 to 21 carbon atoms (the above alkyl group or alkenyl group may be a chain type, or Acids with an alicyclic structure such as higher fatty acids (which may be branched) or resin acids are used; specific examples of these include caprylic acid, capric acid, lauric acid, myristic acid, Valmitic acid, stearic acid, arachidic acid, hebenic acid, isopalmitic acid, isomyristic acid, isostearic acid, undecylenic acid, oleic acid, myristoleic acid, elaidic acid, erucic acid, linoleic acid, linolenic acid, arachidonic acid, coconut oil Fatty acid, beef fatty acid, resin#
(abietic acid), etc. In the following description, for the sake of simplicity, these will be described as higher fatty acids or higher fatty acid side components, including resin acids.

To acylate the plant protein polypeptide obtained as described above, it is sufficient to condense the plant protein polypeptide with a higher fatty acid, but the most common method is the Schotten-Bauman reaction. (Scho
tten-Baua+ann reaction).

In this reaction, acid chloride derivatives of higher fatty acids to be condensed are added to an aqueous solution of plant protein polypeptides at pH 8 to IO.
According to this reaction, as shown in the following formula, R+ CCI +H*NHCHC,0LnOH-R,
-C(NH-CH-Co)-nOH+Hcl Hydrochloric acid is generated and the pH decreases, so it is necessary to maintain the pH at 8 to 10 by adding an alkali such as sodium hydroxide or potassium hydroxide while adding acid chloride. The required reaction time is 1 to 6 hours, and the reaction temperature is 0 to 60°C.
, preferably 20 to 50°C.

As the higher fatty acid side component, in addition to the above-mentioned acid chlorides, acid halides of higher fatty acids such as bromine (Br) and iodine (1) can be used. However, acid chlorides are the most common.

In addition, for commonly used fatty acids having 8 to 22 carbon atoms, in addition to the above-mentioned method using acid halides, it is possible to combine vegetable protein polypeptides with higher fatty acids or lower fatty acids such as their methyl esters and ethyl esters at high temperatures of 150 to 200°C and under high pressure. A method of dehydration condensation or dealcoholization condensation after treatment with an alcohol ester can also be adopted, but this method is not necessarily preferable because the product is colored because it involves high-temperature treatment.

Furthermore, using reagents used for peptide synthesis, higher fatty acids such as N-oxysuccinimide ester, N-
A method of making a carboxyl group-active derivative such as -phthalimide ester and reacting it with a plant protein polypeptide can also be adopted, but this method is expensive and, in addition, the reaction with acid halides is not very reactive.

In any case, the obtained acylated product is preferably released into an aqueous solution of a strong acid such as hydrochloric acid or sulfuric acid, and the liberated product is collected as a floating precipitate, which is purified by washing with water. It can be mixed into a salt form, dissolved in water or a solvent such as alcohol or propylene glycol to form a solution at a desired concentration (10-60%, especially 20-40%), or dried and made into a powder. put to use.

The acylated plant protein polypeptide represented by the above general formula (1) or its salt is incorporated into various cosmetics instead of or in combination with conventional cosmetic formulations.

Cosmetics containing the acylated plant protein polypeptide represented by the above general formula (I) or its salt include, for example, shampoo hair rinse, split end coat, i1 荊 for permanent waving, and second agent for permanent waving. , hair cream, aerosol foam, hair conditioner, setting low silane, hair color, hair color, hair treatment, hair treatment rinse, liquid hair conditioner (low silan), hair bank, hair tonic, hair growth/Aoge Jing Hair cosmetics, lotions, aftershave lotions, shaving foams, vanishing creams, cleansing creams, emollient creams, cold creams, moisture creams, hand creams, facial cleansing creams, hair removal agents, face masks, emulsions, body creams, etc. Various cosmetics can be listed, such as shampoo, various soaps, makeup products, and sunscreen products.

The content thereof is preferably about 0.1 to 20% in terms of pure conversion content in the cosmetic composition.

In addition, examples of ingredients that can be added to the above cosmetics in combination with the acylated plant protein polypeptide represented by general formula (1) or its salt include ammonium lauryl sulfate, ethanolamine lauryl sulfate, sodium lauryl sulfate, and trisulfate lauryl sulfate. Alkyl sulfates such as ethanolamine, polyoxyethylene (2EO) lauryl-thyl sulfate triethanolamine (EO is ethylene oxide, and the number before EOO indicates the number of moles of ethylene oxide added), polyoxyethylene (3EO)
) Alkyl (any one having 11 to 15 carbon atoms or a mixture of two or more 11!I) Alkyl such as polyoxyethylene alkyl ether sulfate such as sodium ether sulfate, sodium laurylbenzenesulfonate, triethanolamine laurylbenzenesulfonate Henzensulfonate, polyoxyethylene alkyl ether acetate such as polyoxyethylene (3EO) tridecyl ether sodium acetate, coconut oil fatty acid sarcosine sodium,
Lauroylsarcosine triethanolamine, lauroylmethyl-β-alanine sodium, lauroyl-L-
N- such as sodium glutamate, lauroyl-glutamate triethanolamine, coconut oil fatty acid-sodium L-glutamate, coconut oil fatty acid-L-glutamate triethanolamine, sodium coconut oil fatty acid methyltaurate, sodium lauroylmethyltaurate, etc.
Acyl amino acid salt, sodium ether sulfate alkanesulfonate, hydrogenated coconut oil fatty acid monosodium glutamate,
Disodium randecylenoylamide ethyl sulfosuccinate, sodium octylphenoxyjethoxyethyl sulfonate, disodium oleic acid amide sulfosuccinate, dioctyl sodium sulfosuccinate, uryl disodium sulfosuccinate, polyoxyethylene alkyl (12 to 15 carbon atoms) Ether phosphoric acid (8~10E
O) Sodium polyoxyethylene oleyl ether phosphate, sodium polyoxyethylene cetyl ether phosphate, disodium uryl polyoxyethylene sulfosuccinate, sodium polyoxyethylene lauryl ether phosphate, sodium lauryl sulfoacetate, sodium tetradecene sulfonate, etc. anionic surfactants, distearyldimethylammonium chloride, dipolyoxyethyleneoleylmethylammonium chloride, stearyldimethylbenzylammonium chloride, stearyltrimethylammonium chloride, cetyltrimethylammonium chloride, tri(polyoxyethylene)stearylammonium chloride, polyoxyethylene chloride Cationic surfactants such as oxypropylenemethyldiethylammonium, myristyldimethylbenzylammonium chloride, lauryltrimethylammonium chloride, 2-alkyl-N-carboxymethyl-N-hydroxyethylimidazolinium betaine, undecylhydroxyethylimidazolium betaine sodium , undecyl-N-hydroxyethyl-N
-Carboxymethylimidazolinium betaine, stearyl dihydroxyethyl betaine, stearyl dimethylamine acetate betaine, coconut oil alkyl betaine, coconut oil fatty acid amidopropyl hetaine, coconut oil alkyl N-carboxyethyl-N-hydroxyethylimidazolinium Sodium betaine, Coco alkyl N-carboxyethoxyethyl-N-carboxyethyl imidazolinium disodium hydroxide, Coco alkyl N-carboxymethoxyethyl-N-carboxymethyl imidazolinium disodium lauryl sulfate, N-coconut fatty acid Ampholytic surface active side such as acyl L-arginine ethyl DL-pyrrolidone carboxylate, polyoxyethylene alkyl (12 to 14 carbon atoms) ether (7EO), polyoxyethylene octylphenyl ether, polyoxyethylene oleyl ether, polyoxy Ethylene glyceryl oleate, polyoxyethylene stearyl ether,
Polyoxyethylene cetyl ether, polyoxyethylene cetyl stearyl diether, polyoxyethylene sorbitol lanolin (40EO), polyoxyethylene nonylphenyl ether, polyoxyethylene polyoxypropylene cetyl ether, polyoxyethylene polyoxybrobylene decyltetradecyl Nonionic surfactants such as ether, polyoxyethylene lanolin, polyoxyethylene lanolin alcohol, polyoxypropylene stearyl ether, cationized cellulose,
Synthetic polymers such as cationic hydroxyethylcellulose, poly(diallyldimethylammonium chloride), polyvinylpyridine, polyethyleneimine, amphoteric polymers, anionic polymers, isostearic acid jetanolamide, undecylenic acid monoethanolamide, oleic acid Tanolamide, bovine fatty acid monoethanolamide, hydrogenated bovine fatty acid jetanolamide, stearic acid jetanolamide, stearic acid diethylaminoethylamide, stearic acid monoethanolamide, myristic acid jetanolamide, coconut oil fatty acid ethanolamide, coconut oil fatty acid gel Thickeners such as tanolamide, lauric acid isopropanolamide, lauric acid ethanolamide, lauric acid jetanolamide, lanolin fatty acid jetanolamide, waxes, paraffins, fatty acid esters, glycerides,
Fats and oils such as animal and vegetable oils, animal and vegetable extracts, polysaccharides or their derivatives, linear or cyclic methylpolysiloxane, methylphenylpolysiloxane, dimethylpolysiloxane polyethylene glycol copolymer, dimethylpolysiloxane polypropylene copolymer, amino-modified silicone oil, silicone oil such as quaternary ammonium modified silicone oil, propylene glycol, 1.3-
Wetting agents such as butylene glycol, ethylene glycol, glycerin, polyethylene glycol, ethanol,
Lower alcohols such as methanol, propyl alcohol, isopropyl alcohol, L-aspartic acid, L
Examples include amino acids such as sodium aspartate, DL-alanine, L-arginine, glycine, L-glutamic acid, cysteine, and L-threonine.

〔Example〕

Next, the present invention will be explained in more detail with reference to Examples.

Example 1 129 g of myristic acid chloride (1.0 equivalent of soy protein polypeptide) was added to 500 g of a 30% aqueous solution of soy protein polypeptide having an average molecular weight of 300 (n"2) over 2 hours while stirring at a constant temperature of 40°C. During that time, the pH of the reaction solution was maintained at 9.0 by appropriately dropping a 20% aqueous sodium hydroxide solution.After stirring at 40°C for 1 hour, the temperature was raised to 50°C, and the reaction was stirred for 1 hour. has ended.

The reaction mixture was discharged into a 5% aqueous sulfuric acid solution 51, and the produced acylated product was suspended in a free form (the form of -COOH in which the carboxylic acid of bebutide is not a salt), washed with water, and then poured into a 30% potassium hydroxide solution. Neutralize by adding
893 g of a 30% aqueous solution of potassium salt of a condensate of soybean protein polypeptide and myristic acid was obtained. Yield is 96
%Met.

The obtained product was confirmed as follows.

Regarding the 30% aqueous solution of the obtained product, amino nitrogen was measured by the Van 5lake method and found to be 0.180 mg/g.

The 30% aqueous solution of soy protein polypeptide used as a raw material had an amino nitrogen content of 14.7 mg/g.
It was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after the nitrogen gas was replaced, the test tube was sealed and heated at 110°.
Hydrolysis was carried out at C for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the soybean protein polypeptide used as the raw material. N the ether layer according to the usual method.
- After methyl esterification using -methyl-N-nitroso-p-toluenesulfonamide, gas chromatography revealed that it was exactly the same as the methyl ester of mystyric acid, the raw material that had been similarly treated and methyl esterified. It turned out to be.

From the above results, it was confirmed that the product was a potassium salt of a condensate of myristic acid at the amino group of the soybean protein polypeptide used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG. The analysis conditions for gas chromatography in this Example 1 and the analysis conditions for gas chromatography in Examples 2 to 8 described later are summarized as follows.

Column: DEI:, S (diethylene glycol succinate)) + Hz PO- (10: 1), inner diameter 3 mm x length 2 m (Examples 1 to 7 and their raw materials), silicone 5E30, inner diameter 3 mm x length 2 m ( Example date and its raw materials) Gas: Nitrogen C30d/min) Detection: Flame ionization detection method Regarding the temperature, 0 is shown in each figure.The number of each peak in the figure indicates the peak detection time (minutes).

Example 2 Coconut oil fatty acid (mixed fatty acid having 8 to 18 carbon atoms) chloride 1 instead of myristic acid chloride in Example 1
Coconut oil fat # of soy protein polypeptide with a concentration of 30% was carried out in the same manner as in Example 1 except that 20 g (1.0 equivalent of soy protein polypeptide) was used and triethanolamine was used in place of potassium hydroxide. 1,090 g of a triethanolamine salt aqueous solution of I condensate was obtained. Yield is 94
%Met.

The obtained product was confirmed as follows.

Amino nitrogen was determined by the Van Slake method for a 30% aqueous solution of the obtained product, and it was found to be 0.16.
It was 5 mg/g. The 30% aqueous solution of soy protein polypeptide used as a raw material contains amino nitrogen i7.4.
mg/g, indicating that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after the nitrogen gas was replaced, the test tube was sealed and heated at 110°.
Hydrolysis was carried out at C for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and extraction was performed by separating into an aqueous layer and an ether layer using a separating funnel. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the soybean protein polypeptide used as the raw material. When the ether layer was methyl esterified using N~methyl-N-nitroso-p-1-luenesulfonamide according to a conventional method, the composition was exactly the same as that of the raw material methyl ester of coconut oil fatty acid, which was similarly treated and methyl esterified. It turned out to be from.

From the above results, it was confirmed that the product was a triethanolamine salt of a condensate of coconut oil fatty acid (mixed fatty acid having 8 to 18 carbon atoms) in the amino group of the soybean protein polypeptide used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 3 47 g of palmitic acid chloride (0.95 equivalent of wheat protein polypeptide) was added to 500 g of a 30% aqueous solution of wheat protein polypeptide having an average molecular weight LOOO (n=7) over 2 hours while stirring at a constant temperature of 45°C. dripped. During that time, the pH of the reaction solution was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After further stirring at 45°C for 1 hour, the temperature was raised to 50°C and stirring was continued for 1 hour to complete the reaction.

The reaction mixture was released into a 5% sulfuric acid aqueous solution 5f to liberate the generated acylated product, and after washing the suspended matter with water, it was neutralized by adding 30% aqueous ammonia to form the ammonium salt of the palmitic acid condensate of wheat protein polypeptide. 30% aqueous solution 543
I got g. The yield was 92%.

The obtained product was confirmed as follows.

The suspended matter (dry residue 34.85%) of the obtained product before being neutralized with 30% ammonia water was
When amino nitrogen was determined by the Slake method, it was found to be 0.
It was 092 mg/g. In addition, the amino nitrogen was measured on the sample before neutralization with 30% aqueous ammonia because after neutralization, the amino group of ammonia is measured, so it cannot be used as a measurement sample for amino nitrogen. be. The 30% water 78 solution of wheat protein polypeptide used as a raw material contains 5.0 mg/g of amino nitrogen.
It was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, and after summer exchange with china gas, the test tube was sealed and heated at 110°.
Hydrolysis was carried out at C for 24 hours. After opening the container and removing hydrochloric acid under reduced pressure i@m, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the wheat protein polypeptide used as the raw material. The ether layer was methyl esterified using N-methyl-N-nitroso-P-toluenesulfonamide according to a conventional method, and gas chromatography was performed. It turned out to be exactly the same as methyl ester.

From the above results, it was confirmed that the product was an ammonium salt of a condensate of palmitic acid at the amino group of the wheat protein polypeptide used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 4 Same as Example 3 except that 36.0 g of underunyl chloride (1.0 equivalent of wheat protein polypeptide) was used in place of palmitic acid chloride in Example 3, and potassium hydroxide was used in place of 30% aqueous ammonia. In the same manner as in 3, 564 g of a 30% aqueous solution of potassium salt of undecylenic acid condensate of wheat protein polypeptide was obtained. Yield is 9
It was 4%.

In addition, fI of the obtained product! The verification was performed as follows.

Amino nitrogen was determined by the Van Slake method for a 30% aqueous solution of the obtained product, and it was found to be 0.11.
It was 7 mg/g. The 30% aqueous solution of wheat protein polypeptide used as a raw material contains 5.5% amino nitrogen.
0 mg/g, indicating that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 4N methanesulfonic acid was added thereto, the tube was replaced with nitrogen gas, the test tube was sealed, and hydrolysis was carried out at 110° C. for 12 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and extraction was performed by separating into an aqueous layer and an ether layer using a separating funnel. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the wheat protein polypeptide used as the raw material. After methyl esterifying the ether layer using N-methyl-N-nitroso-p-1 luenesulfonamide according to a conventional method,
When gas chromatography was performed, methyl ester of undecylenic acid, a raw material that had been similarly treated and methyl esterified, was found (it turned out that they were the same substance).

From the above results, it was confirmed that the product was a potassium salt of a condensate of undecylenic acid at the amino group of the wheat protein polypeptide used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 5 75 g of isostearic acid chloride (0.95 equivalent of soy protein polypeptide) was added dropwise to 500 g of a 30% aqueous solution of soy protein polypeptide having an average molecular weight of 600 (n-4) over 3 hours while stirring at a constant temperature of 40°C. did. During that time, the pH after the reaction was maintained at 9 by appropriately adding a 20% aqueous sodium hydroxide solution. After further stirring at 40°C for 1 hour, the temperature was raised to 45°C and stirring was continued for 1 hour to complete the reaction.

The reaction mixture was diluted with 5% aqueous sulfuric acid solution 5j! 2-amino-
Neutralize with 2-methyl-1,3-propanediol and add ethyl alcohol to prepare 2-amino-2-methyl-1, isostearic acid condensate of soy protein polypeptide.
1,040 g of 25% ethyl alcohol aqueous solution Wi of 3-propanediol salt was obtained. The concentration of ethyl alcohol is 50%.

The yield was 91%.

The obtained product was confirmed as follows.

The resulting product was suspended before neutralization with 2-amino-2-methyl-13-propanediol (dry residue 43
．． 17%), the amine nitrogen content was determined by the Van Slake method and was found to be 0°203/g.

Note that the measurement of aminonitrogen was performed on the sample before neutralization with 2-amino-2-methyl-1,3-propanediol.
This is because the amino group of 3-propanediol is measured, so it cannot be used as a measurement sample for amino nitrogen.

The 30% aqueous solution of soybean protein polypeptide used as a raw material had an amino nitrogen content of 7.3 μ/g, and it was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, nitrogen gas was replaced, the test tube was sealed, and the temperature was heated to 120°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the soybean protein polypeptide used as the raw material. The ether layer was converted into N-
After methyl esterification using methyl-N-nitroso-P-toluenesulfonamide, gas chromatography revealed that it was exactly the same as the raw material methyl ester of isostearic acid that had been similarly treated and methyl esterified. It turns out that there is something.

From the above results, fi! the product is a 2-amino-2-methyl-1,3-propanediol salt of a condensate of isostearic acid at the amino group of the soybean protein polypeptide used as a raw material. It has been certified. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in Table 5.
As shown in the figure.

Example 6 74.4 g of oleic acid chloride (0.8 equivalent of soybean protein polypeptide) was used in place of isostearic acid chloride in Example 5, and 2-amino-2-methyl-1,3-propanediol was used in place of 2-amino-2-methyl-1,3-propanediol. 644 g of a 30% aqueous solution of the sodium salt of the oleic acid condensate of soybean protein polypeptide was obtained in the same manner as in Example N5, except that sodium hydroxide was used and ethyl alcohol was not used. The yield was 91%.

The obtained product was confirmed as follows.

Amino nitrogen was determined by the Van Slake method for a 30% aqueous solution of the obtained product, and it was found to be 0.13.
It was 6■/g. The 30% aqueous solution of soy protein polypeptide used as a raw material contains 7.3 μg of amino nitrogen/g.
It was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 4N methanesulfonic acid was added thereto, the tube was replaced with nitrogen gas, the test tube was sealed, and hydrolysis was carried out at 110° C. for 12 hours. After opening the container and removing hydrochloric acid by condensation under reduced pressure, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. Amino acid analysis of the aqueous layer as a sample revealed that it had the same composition as the soybean protein polypeptide used as the raw material. The ether layer was methyl esterified using N-methyl-N-nitroso-p-)luenesulfonamide according to a conventional method, and gas chromatography was performed. It turned out to be exactly the same as the methyl ester of oleic acid.

From the above results, it was confirmed that the product was a sodium salt of a condensate of oleic acid at the amino group of the soybean protein polypeptide used as a raw material. The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

Example 7 7.8 g of coconut oil fatty acid chloride (1.0 equivalent of wheat protein polypeptide ) was added dropwise over 2 hours. During this time, the pH of the reaction solution was maintained at 9 by appropriately adding a 20% aqueous potassium hydroxide solution. After further stirring at 35°C for 1 hour, the temperature was raised to 45°C and stirring was continued for 1 hour to complete the reaction.

The reaction mixture was released into a 5% aqueous sulfuric acid solution 5β, the generated acylated product was suspended in free form, and the suspended product was washed with water and dissolved by adding propylene glycol to obtain 25% of the coconut oil fatty acid condensate of wheat protein polypeptide. % propylene glycol aqueous solution was obtained. The concentration of propylene glycol is 40%. The yield was 97%.

The obtained product was confirmed as follows.

Regarding the 25% propylene glycol aqueous solution of the obtained product, the amino chinogen was determined by the Van Slake method and found to be 0.092 .mu./g.

The 30% aqueous solution of wheat protein polypeptide used as a raw material contained 0.94 .mu./g of amino-form tin, and it was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, nitrogen gas was replaced, the test tube was sealed, and 110
Hydrolysis was carried out for 24 hours at 'C. After sealing with rIII and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separating funnel for extraction.

When we conducted amino acid analysis on the aqueous layer as a sample, we found that
It was found that it had almost the same composition as the wheat protein polypeptide used as a raw material. After methyl esterifying the ether layer using N-methyl-N-nitroso-p-toluenesulfonamide using a conventional method, gas chromatography revealed that the raw material coconut treated in the same manner and methyl esterified was It turned out to be exactly the same as methyl ester of oil fatty acids.

From the above results, it was confirmed that the product was a condensation product of coconut oil fatty acid in the amino group of the wheat protein polypeptide used as a raw material. The second result of amino acid analysis
In the table, the results of gas chromatography are shown in FIG.

Example 8 The procedure was the same as in Example 1, except that 151 g of resin acid (rosin-based one containing abietic acid as an earth component) chloride (equivalent to 0.1 g of soy protein polypeptide) was used in place of myristic acid chloride in Example 1. , concentration 30%
8" iLg of an aqueous potassium salt solution of a resin condensate of soybean protein polypeptide was obtained. The yield was 86%.

In addition, fim of the obtained product was performed as follows.

Amino nitrogen was determined by the Van Slake method using a 30% aqueous solution of the obtained product, and it was found to be 0.07.
It was 3■/g. The 30 aqueous solution of soy protein polypeptide used as a raw material contains 14.7 g of amino nitrogen/
g, and it was found that most of the amino groups in the product were acylated.

Next, a small amount of the product was placed in a test tube, 6N hydrochloric acid was added thereto, nitrogen gas was replaced, the test tube was sealed, and the temperature was heated to 110°C.
Hydrolysis was carried out for 24 hours. After opening the container and removing hydrochloric acid by concentration under reduced pressure, water and ether were added, and the mixture was separated into an aqueous layer and an ether layer using a separatory funnel for extraction. Amino acid analysis of the aqueous layer as a sample revealed that it had almost the same composition as the soybean protein polypeptide used as the raw material. The ether layer was converted into N-
When methyl esterified using methyl-N-nitroso-p-toluenesulfonamide, it was found that it had exactly the same composition as the methyl ester of the raw resin acid that was similarly treated and methyl esterified.

From the above results, it was confirmed that the product was a potassium salt of a resin acid condensate in the amino group of the soybean protein polypeptide used as a raw material.

The results of amino acid analysis are shown in Table 2, and the results of gas chromatography are shown in FIG.

The cystic acid included in Table 2 is produced by partial oxidation of cystine during hydrolysis or acylation of plant proteins.

The results of amino acid analysis of the acylated plant protein polypeptides or salts thereof obtained in Examples 1 to 8 above are summarized in Table 2 below.

Next, an application example of the present invention will be explained.

Application Example 1 A shampoo having the following composition containing the potassium salt of the myristic acid condensate of the soybean protein polypeptide obtained in Example 1 was prepared, and this was designated as Example 1 of the present invention. In addition, if the ingredient concentration is not added in parentheses after each substance name, it is the blended amount after pure fraction conversion. Furthermore, the amounts of each component are expressed in weight percent. The same applies to the following.

Soybean protein polypeptide of Example 1 15.0 Potassium salt of tonomyristic acid condensate (30%) 2-Alkyl-carboxymethyl-15,ON-hydroxyethylimidazolium hetaine (30%) Coconut oil fatty acid methyl taurine sodium 5.0 um (30%) Coconut oil fatty acid jetanolamide 2.5 Cationized cellulose 0.4 Baroxybenzoic acid ester/feed 0.5 Tsukiji ethanol mixture (Secept manufactured by Acid Co., Ltd.) Olive oil 0.8 Flavor Appropriate amount Sterilized ion-exchanged water Adjusted to pH 6 with malic acid to a total of 100.0 Also, in place of the potassium salt of the myristic acid condensate of soybean protein polypeptide in Example 1 in the above-mentioned Noyanbu, the myristic acid condensate of collagen polypeptide was used. Potassium salt (
A shampoo having the same composition was prepared as Comparative Product 1, except that the same amount of Bromois EMP (manufactured by Acid Co., Ltd.) was blended.

A panel of 10 women used Nyanpu of this implementation product 1 and comparison product 1, and compared the ease of foaming, fineness of the foam, cleaning power, smoothness of hair after washing, combability, and combability. did. The results are shown in Table 3. The results are based on the number of people who answered that product 1 was better;
It is shown by the number of people who answered that Comparison Product 1 was better and the number of people who answered that they were undecided.

As shown in Table 3, the shampoo of Example 1, which contained the potassium salt of the myristic acid condensate of soybean tanno-kuripetide of Example 1, contained the potassium salt of the myristic acid condensate of collagen polypeptide. Compared to the shampoo of Comparative Product 1, the shampoo's ease of foaming, fineness of foam, and detergency were clearly superior. It also has the effect of improving the smoothness, shine, and combability of hair after washing.
Implementation product 1 was better.

Application Example 2 A shampoo having the following composition containing the ammonium salt of the palmitic acid condensate of the wheat protein polypeptide obtained in Example 3 was prepared, and this was designated as Example 2 of the present invention.

Wheat protein polypeptide of Example 3 Ammonium salt of palmitic acid condensate (30%) 20.0 N-Lauroyl-glutamic acid 5.0 Sodium Coconut oil fatty acid Methyl taurate 12.0 Um (30%) Stearin Diethylaminoethyl acid 0.4amide Lauric acid jetanolamide Stearyldimethylbenzyl ammonium chloride (25%) Dimethylsiloxine/methyl (polyoxyethylene) siloxane/methyl (polyoxypropylene) siloxane copolymer (Silicon 5H3749 manufactured by Toray Silicone Co., Ltd.) ) Octamethyl cyclotetrasiloxane biroctone olamine polyoxyethylene (20) nonylphenyl ether baloxybenzoic acid ester/phenoxyethanol mixture (Seisebut, manufactured by Acid Co., Ltd.) Caisson CC, (Protect l1Il!Il, manufactured by Rohm and Haas Japan Co., Ltd.) ) Ethyl sulfate lanolin fatty acid aminopropylene ethyl dimethyl ammonium (cation LQ manufactured by Sanyo Chemical Co., Ltd.) Fragrance Appropriate amount of sterilized ion exchange water Total to 100.0 Also, ammonium salt of the palmitic acid condensate of the wheat protein polypeptide of Example 3 above A shampoo having the same composition as Example 2 was prepared, and this was designated as Comparative Product 2, except that the feces and sterilized ion-exchanged water were not added.

The shampoos of Example Product 2 and Comparative Product 2 were used by 10 female panelists and evaluated in the same manner as in Application Example 1. The results are shown in Table 4.

Table 4 As shown in Table 4, the shampoo of Example 2 containing the ammonium salt of the palmitic acid condensate of the wheat protein polypeptide of Example 3 was formulated with the valmitin 611w1 condensate of the wheat protein polypeptide of Example 3. Compared to comparison product 2 shampoo that does not contain ammonium salts,
The shampoo's ease of lathering, fineness of the foam, and cleaning power were clearly excellent. In addition, the shampoo of Example 2 was also more effective in improving the smoothness, shine, and combability of the hair after washing.

Application Example 3 A shampoo having the following composition containing the potassium salt of the undecylenic acid condensate of the wheat protein polypeptide obtained in Example 4 was prepared, and this was designated as Example 3 of the present invention.

Wheat protein polypeptide of Example 4 35.0 d undecylenic acid Potassium salt of metal (30%) Coconut oil fatty acid amidoprobyl dimethyl 1.5-aminoacetic acid betaine (30%) Cetyltrimethylammonium chloride 0.25 sulfosuccinic acid Polyoxyethylene 4.0 Lauroylethanolamide ester disodium coconut oil fatty acid jetanolamide 1.2 Lauric acid diethanolamide 0.8 Diethylaminoethyl stearate 0.2 Amide dimethyl polysiloxane (Toreshi 0.2 manufactured by Ricon S H2O0- 500cs) Polyoxyethylene (120) Methyl 0.5 Glucoside Diolate Cationized Cellulose (Lion Co., Ltd. 0.3 Leogaide MLP) Ethylene Glycol Monostearate 0.6 Toparaoxybenzoic Acid Ester Fe 0.5 Tsukiji Engineering Tanol mixture (Seisebut manufactured by Acid Co., Ltd.) Flavor Appropriate amount EDTA-2Na O,1 Sterile ion exchange water Total 100
In place of the potassium salt of the undecylene #condensate of the wheat protein polypeptide in Example 4 in the above shampoo, the same amount of the potassium salt of the undecylene sn compound of the collagen polypeptide (Bromois E [JP, manufactured by Acid Co., Ltd.) was added. Except for this, a shampoo having the same composition as in the case of Example Product 3 was prepared, and this was designated as Comparative Product 3.

The shampoos of Example Product 3 and Comparative Product 3 were used by 10 female panelists and evaluated in the same manner as in Application Example 1. The results are shown in Table 5.

Table 5 As shown in Table 5, the shampoo of Example 3 containing the potassium salt of undecylenic acid bath metal of the wheat protein polypeptide of Example 4 contains the potassium salt of undecylenic acid bath metal of the collagen polypeptide. Compared to the shampoo of Comparative Device 3, the shampoo was superior in ease of foaming, fineness of the foam, and detergency.

Application Example 4 A hair rinse having the following composition containing the triethanolamine salt of the coconut oil fatty acid condensate of the soybean protein polypeptide obtained in Example 2 was prepared, and this was designated as Example 4 of the present invention.

Soybean protein polypeptide of Example 2 Triethanolamine salt (30%) of coconut oil fatty acid condensate of 4.5 degrees Trimethyl quaternary ammonium derivative 2.0 collagen polypeptide (30%) (bromois manufactured by Acid Co., Ltd. W-42Q) Hexadecyl stearate 5,5 ethylene glycol distearate 4.5 diethylaminoethyl stearate 3,8 amide diglycerin monoisostearate 3,5 polyoxyethylene (20) cetyl ether 2.0-Tyl dimethyl poly Siloxane (KF 96-350 cs manufactured by Shin-Etsu Siri 0.1 Co., Ltd.) Cetyl alcohol 1.0 Beef tallow alkyl POE (
60) Ether 0.3 myristyl ethylene glycol (Elphakos GT282 manufactured by Lion Corporation) N-cocoyl-L-arginine ethyl 0.2 ester pyrrolidone carboxylate (CAE manufactured by Ajinomoto Co.) Parahydroxybenzoic acid ester 0.3 ester Noxyethanol mixture (Ceicebut manufactured by Acidhu Kasei Co., Ltd.) Fragrance Sterilized ion-exchanged water 100.0 in total Citric acid Adjusted to pH 5.5 In addition, the coconut oil fatty acid condensate of soybean protein polypeptide of Example 2 A hair rinse having the same composition as Example 4 was prepared, and this was used as Comparative Product 4, except that no triethanolamine salt was added and the amount of sterilized ion-exchanged water was increased.

The hair rinses of Example 4 and Comparative Product 4 were diluted 5 times and used on the hair after washing with a commercially available shampoo, and the gloss, suppleness, and combability of the hair were evaluated by a panel of 10 women.
It was evaluated by The results are shown in Table 6.

Table 6 As shown in Table 6, the hair rinse of Example 4 containing the triethanol salt of the coconut oil fatty acid condensate of the soybean protein polypeptide of Example 2 is different from the soybean protein polypeptide of Example 2. Compared to the hair rinse of Comparative Product 4, which did not contain the triethanol salt of the coconut oil fatty acid condensate L7, it was more effective in improving hair frizz, suppleness, and combability.

In particular, the hair rinse of Example 4 is easy to prepare due to the excellent emulsifying power of the triethanolamine salt of the coconut oil/fat am compound of the soybean protein polypeptide of Example 2, and It had excellent storage stability.

Application example 5 2-amino-2-methyl-1,3- isostearic acid condensate of soybean protein polypeptide obtained in Example 5
A hair rinse having the following composition containing a propanediol salt was prepared, and this was designated as Product 5 of the present invention.

Example 50 2-amino-2-methyl-1,3-propanediol salt (30%) of isostearic acid condensate of soybean protein polypeptide 3.0 chloride Diisopropyl adipate 3.0 2.0 Cetyl alcohol 0.3 chloride Cetyltrimethylammonium 6.7 (27%) Distearyldimethylammonium chloride 3.8um (
73%) Dimethylpolysiloxane (K F 96-350 cs manufactured by Shin-Etsu Siri 0.5 Co., Ltd.) Hydrolyzed collagen (30%) (Acid phase 2.0 Bromois W-32R manufactured by Kasei Co., Ltd.) Propylene glycol 3. 0% hydroxybenzoic acid ester/0.3% fluorohydroxybenzoic acid ester/0.3% hydroxybenzoic acid ester mixture (Seisebut, manufactured by Akufu Kasei Co., Ltd.) Fragrance Appropriate amount of sterilized ion-exchanged water To make a total of 100.0% In addition, the isostearin #condensation of the keratin oxidized peptide of Example 5 above A hair rinse with the same composition as Example 5 was used, except that 2-amino-2-methyl-1,3-propanediol salt was not added and the amount of sterilized ion-exchanged water was increased. This was prepared as Comparative Product 5.

When the hair rinses of Example Product 5 and Comparative Product 5 were diluted 5 times and used on hair after washing with a commercially available shampoo to compare the feeling of use, it was found that the hair rinse of Example Product 5 was better. It has excellent effects on improving hair shine, suppleness, and combability, and is easy to prepare as a hair rinse.
Moreover, the storage stability after preparation was excellent.

Application Example 6 A styling mousse base having the following composition containing the sodium salt of the oleic acid condensate of the soy protein polypeptide obtained in Example 6 was prepared, and the styling mousse base and liquefied petroleum gas (LPG) were mixed. 90:10
Fill it into a spray container and use it as a styling mousse.
This was designated as actual product 6 of the present invention.

Soybean protein polypeptide of Example 6 5.0 Sodium oleic acid condensate (30%) Polyoxyethylene (15) Lauryl 0.5 Ether 99% ethanol 5.0 Polyethylene glycol (14) Ole 1.0 Acrylic resin alkanolamine liquid 3.0 Cetyltrimethylammonium chloride 0.5 (29%) Dimethylsiloxane/methyl (poly 1.0 oxyethylene/polyoxypropylene) siloxane copolymer (manufactured by Toray Silicone Co., Ltd. 5H3749) Parahydroxybenzoin Acid ester / 0.3 fluorocarbonoxyethanol mixture (Seisebut, manufactured by Akufu Kasei Co., Ltd.) EDTA-2Na 0.1 fragrance Appropriate amount of sterilized ion exchange water To make a total of 100.0 In addition, the olein of the keratin oxidized peptide of Example 6 above A styling mousse having the same composition as Example 6 was prepared, and this was designated as Comparative Product 6, except that the sodium salt of the acid condensate was not blended and the amount of sterilized ion-exchanged water was increased.

When the styling mousse of this implementation product 6 and comparison product 6 were used on hair and the feeling of use was compared, it was found that the styling mousse of implementation product 6 improved the shine, suppleness, and combability of the hair. The effect was excellent, the styling mousse base was easy to prepare, and the storage stability of the prepared styling mousse was excellent.

Application Example 7 A cream with the following composition containing the wheat protein polypeptide coconut oil fatty acid condensate obtained in Example 7 was prepared,
This was designated as product 7 of the present invention.

Keratin oxidized peptide of Example 7: 4.5 Coconut oil fatty acid tank compound emulsifier mixture (Ayakoru 12.〇-ol 112, manufactured by Akufu Kasei Co., Ltd.) Glycerin monoisostearate 3.0 Hexadecyl isostearate 4.5 Poly Oxyethylene (15) Cetyle 2.0-Tyljojoba oil 1.5 Liquid paraffin 2.5 Dimethylpolysiloxane (Shin-Etsu Siri 0.2 K manufactured by Koichi Co., Ltd.)
F 96-350 cs) Methylphenylbolysiloxane (5H556 manufactured by Higashi 1.5 Resilico Co., Ltd.)
) Butyl parahydroxybenzoate 0.1 Glycerin 9.0 1.3-Butylene glycol 5.0 Triethanolamine 1.0 Retinol palmitate 0.5 Butylated hydroxytoluene
0.05EDTA2-Na
O,1 sterile ion exchange water total 1
00.0 and a cream with the same composition as Example 7, which did not contain the coconut oil fatty acid condensate of wheat protein polypeptide and increased the amount of sterilized ion-exchanged water. was prepared and designated as comparative product 7.

When I used the creams of this implementation product 7 and comparison product 7 on my hands and compared the feel of both products, I found that the cream of implementation product 7 was easier to apply on the skin, spreads better, and leaves the skin shiny and moisturized. The cream was easy to prepare, and the storage stability of the prepared cream was excellent.

Application Example 8 A liquid hair styling product having the following composition containing the potassium salt of the resin acid condensate of the soybean protein polypeptide obtained in Example 8 was prepared and designated as Example 8 of the present invention.

Soybean protein polypeptide of Example 8 3.0 potassium salt of resin acid condensate diisobutyl adipate 0.3 polyoxybrobylene monobutyl ether 23.0-thyl 95% ethanol 63.OO
-Cymen-5-ol 0.1 Propylene glycol 3.0 Fragrance
Appropriate amount of sterilized ion-exchanged water to make a total of 100.0. Also, the soybean protein polypeptide resin N of Example 8 above!
A liquid hair conditioner having the same composition as Example 8 was prepared, and this was designated as Comparative Product 8, except that the condensation alloy potassium salt was not blended and the amount of sterilized ion-exchanged water was increased.

The liquid hair styling products of Example 8 and Comparative Product 8 were each used on the hair of 10 male panelists for one week, and they were asked to evaluate which one was better in terms of hair styling ability, hair gloss, and moisture. The results are shown in Table 7.

Table 7 As shown in Table 7, the liquid hair preparation of Example 8 containing the potassium salt of the resin acid condensate of the soy protein polypeptide of Example 8 is It was more effective in improving iw power, hair gloss, and moisture than Comparative Liquid Hair Conditioner 8, which did not contain a potassium salt of an acid condensate.

〔Effect of the invention〕

As explained above, the acylated product of the plant protein polypeptide represented by the general formula (1) of the present invention or its salt has excellent surfactant ability based on the acylation of the carboxyl group at the terminal end of the peptide. Unlike synthetic surfactants, it is derived from natural plant proteins, so it is less irritating to the skin and hair, and contains the same peptide components as the skin and hair, so it is non-irritating to the skin and hair.・It has an excellent cleaning effect without damaging the skin or hair. Furthermore, the acylated product of the plant protein polypeptide represented by the general formula (1) or its salt has a skin and hair protective action based on the peptide component and an action to regenerate damaged hair. It imparts luster and shine to the skin and improves the combability of hair, so it is used as a compound in hair cosmetics, or as a main ingredient in skin cosmetics such as creams to achieve excellent effects. It is extremely useful as a compounding base.

[Brief explanation of drawings]

Figures 1 to 8 show the results of gas chromatography of the methyl esters of higher fatty acids of the substances obtained in Examples 1 to 8 of the present invention and the methyl esters of higher fatty acids used as raw materials. The temperature and heating rate are as shown in each figure, and the number of each peak in the figure is the detection time (
minutes). Park Kashichikayu 1 Figure 62 Figure Man 3 Figure 4 Figure 5 Figure 6 Figure 7 Figure 8

Claims (1)

[Claims] (1) General formula (I): ▲There are mathematical formulas, chemical formulas, tables, etc.▼ (In the formula, R_1 is an alkyl group with 7 to 21 carbon atoms, an alkenyl group with 7 to 21 carbon atoms, or a hydrocarbon group with an alicyclic structure , R_2 is a side chain of a constituent amino acid of a plant protein polypeptide, n is 2 to 30, and M is hydrogen, an alkali metal such as lithium, sodium, or potassium, ammonium, or monoethanolamine, diethanolamine, triethanol. amine, 2-amino-2-methylpropane, 2-amino-2-methyl-1,3-propanediol, and other organic amines.